An ADP-ribosylating system was detected in a crude homogenate from Sulfolobussolfataricus, a thermophilic archaeon, optimally growing at 87°C. The archaeal ADP-ribosylationreaction was time-, temperature- and NAD-dependent. It proved to be highly thermostable, with about 30% decrease of 14C incorporation from [14C]NAD on incubation at 80°C for up to 24 h. The main reaction product was found to be mono-ADP-ribose. Testing both [adenine- 14C(U)]NAD and [adenine- 14C(U)]ADPR as substrates, it was found that acceptor proteins were modified by ADP-ribose both enzymatically, via ADP-ribosylating enzymes, and via chemical attachment of free ADP-ribose, likely produced by NAD glycohydrolase activity. The synthesis of ADP-ribose-protein complexes was shown to involve mainly acceptors with molecular masses in the 40–100 kDa range, as determined by electrophoresis on polyacrylamide gel in the presence of sodium dodecyl sulphate.
ADP-ribosylation reactions in Sulfolobus solfataricus, a thermoacidophilic archaeon / M., Rosaria Faraone Mennella; Filomena De, Lucia; DE MAIO, Anna; Agata, Gambacorta; Piera, Quesada; Mario De, Rosa; Barbara, Nicolaus; Benedetta, Farina. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY. - ISSN 0167-4838. - STAMPA. - 1246:(1995), pp. 151-159. [10.1016/0167-4838(94)00169-H]
ADP-ribosylation reactions in Sulfolobus solfataricus, a thermoacidophilic archaeon
DE MAIO, ANNA;
1995
Abstract
An ADP-ribosylating system was detected in a crude homogenate from Sulfolobussolfataricus, a thermophilic archaeon, optimally growing at 87°C. The archaeal ADP-ribosylationreaction was time-, temperature- and NAD-dependent. It proved to be highly thermostable, with about 30% decrease of 14C incorporation from [14C]NAD on incubation at 80°C for up to 24 h. The main reaction product was found to be mono-ADP-ribose. Testing both [adenine- 14C(U)]NAD and [adenine- 14C(U)]ADPR as substrates, it was found that acceptor proteins were modified by ADP-ribose both enzymatically, via ADP-ribosylating enzymes, and via chemical attachment of free ADP-ribose, likely produced by NAD glycohydrolase activity. The synthesis of ADP-ribose-protein complexes was shown to involve mainly acceptors with molecular masses in the 40–100 kDa range, as determined by electrophoresis on polyacrylamide gel in the presence of sodium dodecyl sulphate.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
